ID   DER11_MAIZE             Reviewed;         243 AA.
AC   Q4G2J6; Q4G2K0; Q9LEE5;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Derlin-1.1;
DE   AltName: Full=ZmDerlin1-1;
GN   Name=DER1.1; Synonyms=SOR;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. LH132;
RX   PubMed=15849299; DOI=10.1104/pp.105.060087;
RA   Kirst M.E., Meyer D.J., Gibbon B.C., Jung R., Boston R.S.;
RT   "Identification and characterization of endoplasmic reticulum-associated
RT   degradation proteins differentially affected by endoplasmic reticulum
RT   stress.";
RL   Plant Physiol. 138:218-231(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Wisconsin 64A;
RA   Bastida M., Roca R., Cejudo F.J., Stiefel V., Puigdomenech P.;
RT   "A gradient of programmed cell death develops in scutellum during maize
RT   embryogenesis.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the degradation process of specific
CC       misfolded endoplasmic reticulum (ER) luminal proteins.
CC       {ECO:0000269|PubMed:15849299}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15849299}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15849299}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stalks, leaves, immature ears,
CC       embryo and endosperm. {ECO:0000269|PubMed:15849299}.
CC   -!- INDUCTION: By endoplasmic reticulum stress.
CC       {ECO:0000269|PubMed:15849299}.
CC   -!- MISCELLANEOUS: Associated with ER-derived protein bodies in endosperm.
CC   -!- SIMILARITY: Belongs to the derlin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY41612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB97005.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR   EMBL; AY854013; AAY41608.1; -; mRNA.
DR   EMBL; AY854017; AAY41612.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AJ251622; CAB97005.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001105945.1; NM_001112475.1.
DR   AlphaFoldDB; Q4G2J6; -.
DR   SMR; Q4G2J6; -.
DR   STRING; 4577.GRMZM2G117388_P01; -.
DR   PaxDb; Q4G2J6; -.
DR   PRIDE; Q4G2J6; -.
DR   EnsemblPlants; Zm00001eb350050_T004; Zm00001eb350050_P004; Zm00001eb350050.
DR   EnsemblPlants; Zm00001eb350050_T006; Zm00001eb350050_P006; Zm00001eb350050.
DR   GeneID; 100037763; -.
DR   Gramene; Zm00001eb350050_T004; Zm00001eb350050_P004; Zm00001eb350050.
DR   Gramene; Zm00001eb350050_T006; Zm00001eb350050_P006; Zm00001eb350050.
DR   KEGG; zma:100037763; -.
DR   eggNOG; KOG0858; Eukaryota.
DR   OMA; SCKRTIN; -.
DR   OrthoDB; 1609512at2759; -.
DR   Proteomes; UP000007305; Chromosome 8.
DR   ExpressionAtlas; Q4G2J6; baseline and differential.
DR   Genevisible; Q4G2J6; ZM.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   InterPro; IPR007599; DER1.
DR   InterPro; IPR035952; Rhomboid-like_sf.
DR   Pfam; PF04511; DER1; 1.
DR   SUPFAM; SSF144091; SSF144091; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Stress response;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Derlin-1.1"
FT                   /id="PRO_0000249241"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..55
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..157
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          219..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        204
FT                   /note="V -> VR (in Ref. 1; AAY41612)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  27842 MW;  6D4F8A0D42B2966F CRC64;
     MSSPAEYYKS LPPISKAYGT LCFFTTVLVQ LQILHPLFLY LDYPLVFKKF EIWRLLTSFF
     FLAPFSMKFG IRLLMIARYG VMLEKGAFDK RTADFLWMMI FGAISLLVLS IIPLFNSFFL
     GIPMVSMLLY VWSRENPNAQ INIYGLVQLR SFYLPWAMLL LDVIFGSSLM PGLLGIMVGH
     LYYFFAVLHP LATGKSYLKT PKWVHKIVAR FRIGMQANSP VRPPANGNSG SGVFRGRSYR
     LNQ